7NXF

Structure of the fungal plasma membrane proton pump Pma1 in its auto-inhibited state - monomer unit

7NXF の概要

• エントリーDOI: 10.2210/pdb7nxf/pdb
• EMDBエントリー: 12638
• 分子名称: Plasma membrane ATPase, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: membrane protein, p-type atpase, proton-transporting atpase, proton transport
• 由来する生物種: Neurospora crassa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 100474.96

構造登録者

Heit, S.,Geurts, M.M.G.,Murphy, B.J.,Corey, R.,Mills, D.J.,Kuehlbrandt, W.,Bublitz, M. (登録日: 2021-03-18, 公開日: 2021-11-17, 最終更新日: 2025-07-09)

主引用文献

Heit, S.,Geurts, M.M.G.,Murphy, B.J.,Corey, R.A.,Mills, D.J.,Kuhlbrandt, W.,Bublitz, M.
Structure of the hexameric fungal plasma membrane proton pump in its autoinhibited state.
Sci Adv, 7:eabj5255-eabj5255, 2021

PubMed Abstract: The fungal plasma membrane H-ATPase Pma1 is a vital enzyme, generating a proton-motive force that drives the import of essential nutrients. Autoinhibited Pma1 hexamers in the plasma membrane of starving fungi are activated by glucose signaling and subsequent phosphorylation of the autoinhibitory domain. As related P-type adenosine triphosphatases (ATPases) are not known to oligomerize, the physiological relevance of Pma1 hexamers remained unknown. We have determined the structure of hexameric Pma1 from by electron cryo-microscopy at 3.3-Å resolution, elucidating the molecular basis for hexamer formation and autoinhibition and providing a basis for structure-based drug development. Coarse-grained molecular dynamics simulations in a lipid bilayer suggest lipid-mediated contacts between monomers and a substantial protein-induced membrane deformation that could act as a proton-attracting funnel.

PubMed: 34757782
DOI: 10.1126/sciadv.abj5255

実験手法

ELECTRON MICROSCOPY (3.1 Å)